Possible mechanism for Tay-Sachs, thus leading way for easier cure

I propose it may be from a comorbid infection of Streptomyces ( not sure which strain yet,) B. thetaiotaomicron, and Prevotella. The different forms may also be attributable to different combinations of similar species, such as Bacteroides, such as Bacteroides fragilis, and also these conditions seem related to Tannerella forsythia presence as well.



There may be a pathogenic component, especially considering Streptomyces is capable of horizontal gene transfer induction.



Also:
"Amongst N-acetylhexosaminidase inhibitors (Figure 1), 2-acetamido-1,2-dideoxynojirimycin, 1 [10] and diastereomers such as the d-galacto (2) [11] and the d-allo (3) [12] analogs, PUGNAc (4) [13], and NAG-thiazoline (NGT, 5) [14] have attracted considerable attention. Furthermore, Thiamet G (6) [15], nagstatin (7) [16], and 6-acetamido-6-deoxycastanospermine (8) [17], various pyrrolidine derivatives (for example, compound 9 [18]), as well as 2-N-acetyl glycals including 10 [19] have been reported. Amongst carbacyclic hexosaminidase inhibitors, pyranoid carbasugar acetamidodeoxy-β-valienamine (11) has to be mentioned [20]. These inhibitors are either substrate/product analogs or, in the case of bicyclic systems such as NGT, are chemically stable structural analogues of the above-mentioned intermediate generated by anchimeric assistance of the N-acetyl group at C-1 at the first transition state of enzymatic N-acetylhexosaminide hydrolysis. "

www.mdpi.com...

"Streptomyces plicatus by 2-acetamino-1,2-dideoxynojirimycin-lysine hybrids"
www.ncbi.nlm.nih.gov...

"Nagstatin, a new inhibitor of N-acetyl-beta-D-glucosaminidase (NAG-ase) was discovered in the fermentation broth of Streptomyces amakusaensis MG846-fF3. It was purified by chromatography on Dowex 50W, Avicel and Sephadex LH-20 followed by the treatment of active carbon and then isolated as colorless powder. Nagstatin has the molecular formula of C12H17N3O6. It is competitive with the substrate, and the inhibition constant (Ki) was 1.7 x 10(-8) M. "

www.revolvy.com...

"inhibit.
Go to:
DISCUSSION
We report here the identification, characterization, purification, cloning, and expression of a novel enzyme that is able to remove sulfate from mucin oligosaccharide chains by glycosidic cleavage of terminal 6-SO3-β-GlcNAc residues. The enzyme was found in Prevotella strain RS2, an anaerobic bacterium originally isolated from pig colon mucosa. We termed this enzyme a sulfoglycosidase and showed that it differs from the mucin-desulfating sulfatase, MdsA, that has been described previously. The SGL activity is not due to sequential action of MdsA and hexosaminidase. SGL is translocated to the periplasm, as shown by cell fractionation studies and by the presence of a periplasmic translocation motif at the N terminus of the translated product. At least one other fraction catalyzing SGL activity was detected during purification, and we have not investigated yet whether this fraction is a degradation product of the 100-kDa protein or is an isoenzyme.

SGL was tested for activity against a number of model substrates which have structures analogous to the structures of sugars in mucin oligosaccharide chains (Table (Table2).2). Activity was found only with 6-SO3-β-GlcNAc-1-pNP, in agreement with data showing that SGL released free 6-SO3-GlcNAc from mucin. The inability of SGL to cleave pNP from the disaccharide substrate 4-(β-Gal)-6-SO3-β-GlcNAc-1-pNP strongly suggests that the enzyme is an exosulfoglycosidase.

When the translated 901-amino-acid sequence (before translocation of the SGL) was compared with BLAST protein database sequences, the closest matches were with β-hexosaminidases from B. thetaiotaomicron and Porphyromonas gingivalis. To the best of our knowledge, these enzymes have not been isolated and/or have not been tested for activity against sulfated substrates, and SGL activity has not been described previously in bacteria. When crude cell extracts from several common species of gut anaerobes were assayed for SGL-like activity, B. fragilis and B. thetaiotaomicron appeared to have some activity, although the levels were lower than the levels for Prevotella strain RS2. The possible activity detected in P. melaninogenica was most likely due to sulfatase plus hexosaminidase. The nine other isolates tested had no SGL-like activity. It seems likely that some of the uncharacterized members of the CAZy GH20 family may well catalyze SGL-type reactions rather than conventional β-N-acetylhexosaminidase reactions.

Only one other enzyme, human β-d-N-acetylhexosaminidase A, has been shown to remove intact 6-SO3-GlcNAc from 6-SO3-β-GlcNAc-1-pNP. Consistent with this specificity, the human enzyme can liberate 6-SO3-GlcNAc from the nonreducing end of keratan sulfate-derived oligosaccharides. The enzyme can also remove GlcNAc from β-GlcNAc-1-pNP and shows 20-fold-higher affinity for the nonsulfated substrate (10). In contrast, the Prevotella SGL cleaves the nonsulfated substrate at a rate that is only 1% of the rate seen with the sulfated substrate (with substrate at a concentration of 1 mM), and the difference is due to the fact that the nonsulfated substrate has a higher Km and a lower Vmax. The Km and Vmax values are for model substrates, however, and may not necessarily be correct for native substrates. The Prevotella enzyme has a sevenfold-higher affinity (Km = 0.18 mM) for 6-SO3-β-GlcNAc-1-pNP than the human enzyme has. We have not tested the Prevotella SGL with keratan sulfate-derived oligosaccharides.

The human β-d-N-acetylhexosaminidase A is better known for its alternative specificity in cleaving N-acetylgalactosamine from the oligosaccharide chain of GM2 ganglioside. The human recessive lysozomal storage disease (GM2 gangliosidosis) called Tay-Sachs disease (9) results from β-d-N-acetylhexosaminidase A deficiency due to inheritance of mutant forms.

The finding that both a mucin-desulfating sulfatase (MdsA) (28) and SGL are present in the periplasm of Prevotella strain RS2 (and perhaps other bacteria) leads us to propose that sulfate group metabolism in sulfomucins, sulfoglycoproteins, and/or sulfoglycolipids must have important functions in the colonic habitat, which the bacterium is attempting to modify. These enzymes may enhance the ability of the bacterium to survive in its environment. Both enzymes are partially induced by growth on mucin, and both can desulfate mucin. The product of SGL action is a substrate for MdsA sulfatase, but not vice versa. The proposed roles of SGL in mucin metabolism may be hypothesized to be (i) removal of inhibitory 6-SO3-β-GlcNAc groups from mucin chains that limit degradation of the chain by exoglycosidases and neuraminidases, (ii) removal of 6-SO3-β-GlcNAc groups from mucin chains (usually exposing a galactose as the new terminal residue), thus creating or removing sites for different adhesins, and (iii) provision of 6-SO3-GlcNAc as a readily hydrolysable substrate for MdsA sulfatase. The first two roles could have substantial effects on the colon mucosal habitat.

IMPORTANT: Using Content From Other Websites on ATS
Posting work written by others

Continued:
It has been well established that there is a lower sulfate content in secreted colonic mucin in ulcerative colitis patients (6) and that mucin is more susceptible to fecal-bacterial glycosidase action in the presence of added sulfatase (26). The role of the SGL, as well as mucin-specific sulfatase activities, needs to be taken into account when the significance of mucin sulfate levels and the rate of desulfation are considered in relation to mucus barrier effectiveness and susceptibility to degradation. The presence of an enzyme with this selective specificity also suggests that its targeted sulfated sugar may have had an important biological action in its own right before its removal, such as being part of a ligand. Such an action of negatively charged groups on carbohydrate-presenting molecules has been documented in the case of 9-O-acetylsialic acids or sulfate groups in siglec and selectin ligands, the loss of which diminishes or prevents their function."



www.ncbi.nlm.nih.gov...

The pathogens mentioned that share a similar genetic signature to the Prevotella are important, After reading this study, consider the following:

"Neuraminidase-1 contributes significantly to the degradation of neuronal B-series gangliosides but not to the bypass of the catabolic block in Tay–Sachs mouse models"

One mentioned:

en.wikipedia.org...

Consider the elevated levels of sialic acid, and consider this study:

academic.oup.com...



Finally, the similarity to Salla disease and Tay Sachs is rather remarkable: Consider this as well: www.biochemj.org...

Thank you for taking the time to go over this. In summary I'm proposing it may be a congenital pathogenic complex that influences such mutations in the enzymes involved.

The prior research sent elucidated how it came to be a hereditary like condition, also, they may act as triggers as well. All of them surmount to the condition being discussed.


Interaction of Clostridium perfringens δ toxin with erythrocyte and liposome membranes and relation with the specific binding to the ganglioside GM2
Abstract
C. Jolivet-Reynaud, B. Hauttecoeur and J. E. Alouf. Interaction of Clostridium perfringens δ toxin with erythrocyte and liposome membranes and relation with the specific binding to the ganglioside GM2. Toxicon27, 1113–1126, 1989.—The specific interaction of the cytolytic Clostridium perfringens δ toxin with membrane GM2 was indicated by: (i) characterization of this glycolipid in the membrane of sheep and goat erythrocytes, which are lysed by the toxin, whereas GM2 was undetectable in insensitive rabbit erythrocytes, (ii) demonstration of 125I-toxin binding to GM2, by autoradiography, following incubation with thin-layer chromatograms containing separated neuroblastoma gangliosides, and (iii) toxin fixation by phospholipid-cholesterol unilamellar vesicles containing either sheep gangliosides or GM2.

In order to investigate the intramembrane events leading to membrane disruption following toxin binding, the photoreactive probe 12(4-azido-2-nitrophenoxy)stearoyl l-14C glucosamine, which inserts into the outer layer and labels integral membrane proteins, was used to establish whether δ toxin penetrates into target cell membrane. No toxin labeling was found, suggesting that toxin action takes place at the membrane surface. This contention is supported by the observation that despite toxin binding, GM2 liposomes did not release entrapped 14C-glucose. Treatment of toxin with carboxypeptidases, but not aminopeptidases, abolished both toxin binding capacity onto erythrocytes and its combination with antitoxin neutralizing antibodies, suggesting that the carboxy terminal end of the toxin is critical for binding to cell membrane.

www.sciencedirect.com...

(v) C. perfringens type D.Toxinotype D is by far the most common cause of clostridial enterotoxemia in sheep and goats and is occasionally the cause of clostridial enterotoxemia in other animal species (3). ETX is considered to mediate, in large part, the pathogenesis of C. perfringens type D disease; e.g., intravenous ETX injection in sheep and goats has been shown to reproduce most of the clinical signs and lesions of natural diseases in these species (213), and an intravenous ETX monoclonal antibody (MAb) was able to protect mice from intraduodenal challenge with type D strains (214). In enterotoxemia, ETX affects endothelial tight junctions in the brain (215), causing swelling and rupture of perivascular astrocyte processes (216). These effects are followed by increased capillary permeability (217), rapid extravasation of fluid (218), elevated intracerebral pressure, and parenchymal necrosis (215). In most animal species, type D disease is clinically characterized by neurological disease involving perivascular edema of the brain and, less frequently, by focal symmetrical encephalomalacia.

mmbr.asm.org...

We are learning more and more about the toxins produced by various microbial pathogens leading to what were once thought to be genetic conditions. For example:

"Dolphins stranded on the beaches of Florida and Massachusetts show in their brains amyloid plaques, a hallmark in human beings of Alzheimer's disease, together with an environmental toxin produced by cyanobacterial blooms.

An international team of scientists led by neuropathologist Dr. David Davis at the University of Miami Neurology Department discovered that stranded dolphins have both β-amyloid plaques and the environmental toxin BMAA in their brains.

"We found β-amyloid plaques and damaged neurons in brain tissues from dolphins that had died on the beaches of Florida and Massachusetts," Dr. Davis said.

"Dolphins are an excellent sentinel species for toxic exposures in the marine environment," co-author Dr. Deborah Mash explained. "With increasing frequency and duration of cyanobacterial blooms in coastal waters, dolphins might provide early warning of toxic exposures that could impact human health."

Scientists have previously found that chronic dietary exposure to the cyanobacterial toxin BMAA triggers β-amyloid plaques and neurofibrillary tangles, both hallmarks of Alzheimer's disease, in laboratory animals."

www.eurekalert.org...

I think many of these microbial toxins may be mutagenic and therefore contribute to "genetic" abnormalities, ie, congenital diseases.

Oh and also to explain why jacob sheep were mentioned:

www.ntsad.org...

I'd definitely look into what toxins could be present in the soil or food, to see if there is anything that could potentially agonize the underlying mechanism.

It would be interesting to see how identical the Alzheimer's like syndrome present in dolphins is to humans.

That is a little over my head, I can read it but know nothing much about how Tay Sachs works. I haven't studied that enzyme they are talking about much yet, if would be low on my priority since I don't know anyone dealing with that condition personally. I can understand the article but do not know the relevance of how they are counteracting the disease, for now I will admit that is over my head.

Many bacteria have the ability to do horizontal transfer, even between different species is common.

I skipped through the information and did twenty minutes of research, but that is not nearly enough time to figure out how to fix anything. It sounds like a particular lipase is missing, which could be similar to a proteinase in the diet disolving it but there is actually a gene mutation that stops the production of that lipase. I do not think a statin would be the right solution, lowering the excretion of the lipid and absorbtion of the lipid is not solving anything. Eliminating a protease would not work, it seems you would need to add a special lipase to the diet. I would have to research the genes involved in this to get some possible ideas on how to do this. dihydroorotate dehydrogenase doesn't actually sound like a typical lipase though.

originally posted by: rickymouse
That is a little over my head, I can read it but know nothing much about how Tay Sachs works. I haven't studied that enzyme they are talking about much yet, if would be low on my priority since I don't know anyone dealing with that condition personally. I can understand the article but do not know the relevance of how they are counteracting the disease, for now I will admit that is over my head.

Many bacteria have the ability to do horizontal transfer, even between different species is common.

I skipped through the information and did twenty minutes of research, but that is not nearly enough time to figure out how to fix anything. It sounds like a particular lipase is missing, which could be similar to a proteinase in the diet disolving it but there is actually a gene mutation that stops the production of that lipase. I do not think a statin would be the right solution, lowering the excretion of the lipid and absorbtion of the lipid is not solving anything. Eliminating a protease would not work, it seems you would need to add a special lipase to the diet. I would have to research the genes involved in this to get some possible ideas on how to do this. dihydroorotate dehydrogenase doesn't actually sound like a typical lipase though.

Indeed, it may be interesting to see how the gut bacteria in the sheep and humans affected with this differ or share in similarity. There are related diseases that are far more common.

a reply to: ginseng23

Somewhere in the article they mentioned sulfate deficiency may contribute, now the molybdopterins convert sulfites to sulfates in the body. A deficiency in Molybdenum or a messed up MOCO enzyme could be a part of the problem.

a reply to: rickymouse

Very astute observation and conicisement!!

www.nature.com...

You very may have further narrowed down the culprit. Thank you!

"Neisseria meningitidis MC58, using microarray analysis. Target genes that appeared to be regulated by NsrR, based on a comparison between an nsrR mutant and a wild-type strain, were further investigated by quantitative real-time PCR, revealing a very compact set of genes, as follows: norB (encoding NO reductase), dnrN (encoding a protein putatively involved in the repair of nitrosative damage to iron-sulfur clusters), aniA (encoding nitrite reductase), nirV (a putative nitrite reductase assembly protein), and mobA (a gene associated with molybdenum metabolism in other species but with a frame shift in N. meningitidis). "

jb.asm.org...

Although the title disease in question is relatively less common compared to Alzheimers, I believe it will be key into understanding the various pathways in which Microcystins — or cyanoginosins, or any sort of toxin, really, wreak their havoc.

Understanding which types of flora and fauna are more common to a given locality can further pinpoint avenues of treatment for such lysosomal storage disorders.

a reply to: rickymouse

Also, to further support this point:

"Portions of the LPS from several bacterial strains have been shown to be chemically similar to human host cell surface molecules; the ability of some bacteria to present molecules on their surface which are chemically identical or similar to the surface molecules of some types of host cells is termed molecular mimicry.[25] For example, in Neisseria meningitidis L2,3,5,7,9, the terminal tetrasaccharide portion of the oligosaccharide (lacto-N-neotetraose) is the same tetrasaccharide as that found in paragloboside, a precursor for ABH glycolipid antigens found on human erythrocytes.[11] In another example, the terminal trisaccharide portion (lactotriaose) of the oligosaccharide from pathogenic Neisseria spp. LOS is also found in lactoneoseries glycosphingolipids from human cells.[11] Most meningococci from groups B and C, as well as gonococci, have been shown to have this trisaccharide as part of their LOS structure.[11] The presence of these human cell surface 'mimics' may, in addition to acting as a 'camouflage' from the immune system, play a role in the abolishment of immune tolerance when infecting hosts with certain human leukocyte antigen (HLA) genotypes, such as HLA-B35.[11]"

en.wikipedia.org...-antigen

a reply to: ginseng23

Here is a good article about Molybdenum cofactors. lpi.oregonstate.edu...

Another one. lpi.oregonstate.edu...

In the body, the major natural antioxidant is a conditional amino acid, meaning the body can make it. It is taurine. But you need Molybdenum as a cofactor for sulfite oxidase to make it along with ample manganese, Vitamin B6 and selenium. If any of those are not up to par, you cannot make adequate taurine. Meat contains taurine, but sulfite oxidase deficiency also reduces the ability of the body to utilize taurine. Also excess riboflavin in the body hoards the sulfite oxidase. Leaving people with low levels of sulfate and high levels of sulfites. And of course, the molybdem cofactor is utilized for many different enzymes, nitrogen compounds need it for detox, so you need adequate amounts of the MOCO enzymes to process many types of processes. If you consume lots of hot sauce, then you could have a deficiency in taurine utilization and also have elevated sulfite levels. This can lower our ability to fight things.

I take a small supplement, a hundred thirty percent of RDA of Molybdenum, and it is adequate to keep my sulfite levels down so I don't get the sulfite headaches much anymore. Aldehydes are also detoxed by the MOCO pathways, to detox the aldehydes created by metabolizing alcohol, it takes some of the Molybdenum from your system. Molybdenum is stored in the silver skin of meats, and it is in the cartilage, it is used to help with usage of the sulfur contained in the collegan stores to keep bones and teeth strong. Too much molybdenum can cause a copper deficiency, so my multimineral tablet also contains copper, copper enzymes are important to the body. They also make collagen and joints.

I know where this mineral is found in nature, I have actually consumed a lot of these foods on a regular basis all my life. The thing is, genetically, I have a deficiency of a certain type of MOCO enzyme, so I take a little every day and I feel good since it is always available even if the I only make limited amounts of the enzyme. It works, I have been taking a supplement for ten years now, I cannot take a multivitamin, but I do take a special B complex vitamin supplement about four times a week. It has lots of riboflavin though, when I take it I take a boosted molybdenum multimineral that contains limited special mineral complexes. I have been testing on myself for years, some tests taught me not to try it again, like trying to take magnesium supplements for a long time, it caused muscle spasms....I unbalanced the magnesium to the calcium in my body with just a one hundred percent RDA of magnesium for about three weeks. Now I take a twenty five percent magnesium and twenty five percent calcium citrate pill and it stays balanced. Too much calcium without enough magnesium causes issues too, I tried that for a month.....I am not going to even attempt that anymore, I got constipated to hell because it upset the pulsing of my colon, it got stuck on on.

I test on myself a lot to see what will happen. Having the genetic app is a plus, I just need to get a full sequence now to get a better ability to properly identify how epigenetic factors effect this stuff. Next time I can get it for about three hundred bucks, I will get it done. It does require blood being drawn, I will have to get ahold of my daughters doctor who works with that kind of stuff to get a draw.

It is actually fun doing all this research...I know I am OCD and a little crazy but I am very particular with properly evaluating things and it takes a very long time to test on myself. It took me a year to find out positively that I cannot eat a banana the same day as potatoes....it results in me getting allergic to latex in my underwear. So I do not have to buy latex free clothes anymore if I just avoid bananas and avacados and Kiwi.

originally posted by: ginseng23
a reply to: rickymouse

Also, to further support this point:

"Portions of the LPS from several bacterial strains have been shown to be chemically similar to human host cell surface molecules; the ability of some bacteria to present molecules on their surface which are chemically identical or similar to the surface molecules of some types of host cells is termed molecular mimicry.[25] For example, in Neisseria meningitidis L2,3,5,7,9, the terminal tetrasaccharide portion of the oligosaccharide (lacto-N-neotetraose) is the same tetrasaccharide as that found in paragloboside, a precursor for ABH glycolipid antigens found on human erythrocytes.[11] In another example, the terminal trisaccharide portion (lactotriaose) of the oligosaccharide from pathogenic Neisseria spp. LOS is also found in lactoneoseries glycosphingolipids from human cells.[11] Most meningococci from groups B and C, as well as gonococci, have been shown to have this trisaccharide as part of their LOS structure.[11] The presence of these human cell surface 'mimics' may, in addition to acting as a 'camouflage' from the immune system, play a role in the abolishment of immune tolerance when infecting hosts with certain human leukocyte antigen (HLA) genotypes, such as HLA-B35.[11]"

en.wikipedia.org...-antigen

Well, a good proteinase like bromelain will take the mucus off of the cells and reduce inflammation. To soften certain viruses and bacteria, Monolaurin, or lauric acid from coconut oil or butter treated by lipase in the gut can make monolaruin. Milk has monolaurin in it too, human milk has more than cow milk. But when you drink two percent or one percent, the monolaurin is depleted, it is still a lipid. Monolaurin kind of sensitizes cells so our immune system can interact with them. it softens them and it increases pourocity. Our cells can handle this, it doesn't do any harm to them, but it takes away the shield of microbes.

I have read a very lot of research articles about everything, but I find that there are only about twenty different things that can help our body fight things correctly. The thing is, we seem to have been steered away from the stuff that actually makes us healthy. Like eggs. Choline is utilized by the body to properly send and receive instructions to the cells and if you do not have enough choline, you can have a messed up immune response. Choline and betaine are similar but different, I lack the ability to make enzymes to switch one to the other in any quantity due to epigenetic factors. A little I can do, but I have to consume both of these chemicals, I have instinctively eaten these all my life, but when I got older, my physiology changed and so did my automatic cravings. My cravings do not work right anymore. I cannot eat like I could when I was younger, and my cravings do not work as good either, then I had the wife giving me the evil eye every time I pick up the salt shaker, I pee out all my salt, I have to consume at least the maximum RDA of salt, and I do not eat much junk food anymore, so my sodium goes low. The doctor told me to consume more salt because my blood pressure goes too low quite often, my volume is low. Eating too much food with diuretic properties, healthy foods, is not always good.

a reply to: rickymouse

Interesting, which of these do you know to be antimutagenic?

originally posted by: ginseng23
a reply to: rickymouse

Interesting, which of these do you know to be antimutagenic?

That is complicated, for cancer to form, it takes a whole bunch of things to happen. First, cancer causes slime to build up to protect it from immune system detection, a proteinase can help to reduce the mucus, but mucus also has it's function in our lungs and digestive system to protect us from pathogens, moderation should be observed, cycled in the diet. Next, too much copper can cause cancer to grow fast, copper stimulates angeogenasis, with the aid of sulfite oxidase and moco enzymes, copper can be effectively taken down to proper levels. Too little copper is no good either, that can lead to a lot of problems with cartilage and collagen building too, remember, veins are made of collagen too, they need copper to grow. But cancer stimulates copper enzymes to build extra blood vessels in tumors. Molybdenum helps to moderate copper enzymes, too little is no good, too much is no good.

Next is aptopsis, chemicals in food like apigenin and luetening and even narageenan can help to stimulate aptopsis or cell death of damaged cells. So, those are found in some veggies and spices like celery and parsley in higher amounts while narageenan is found in grapefruit and also quercetin, a similar chemical is found in onions and many other veggies, including the skin of apples...skin that is actually covered in pesticides which tend to actually promote mutations to some extent.

Consuming foods containing n-acetyl cysteine can help to boost glutione whic protects good cells, but also protects cancerous cells. It is better to consume this chemistry to protect you from getting cancer, and avoid it if you have cancer growing in you. Gluthione is a lipid like liquid that helps prevent oxydation in the cells.

The electrolytes, sodium and chloride open the sodium channels which allows the cell to lose fluids which contain metabolites of cell energy that need to be excreted, sodium and chloride shuffle the toxins out of the body through the kidneys. If there is not enough of these electrolytes, then the toxins build up in the cells and it causes the oxydation of the DNA to increase and increases damage. Within the cells, potassium is more abundant along with magnesium, so these help shuffle things within the cells to the sodium receptors for excretion. Calcium and glutamate work as ion pumps on other receptors to supply energy, Again, too much or too little of these substances is no good, adjusting them should incorporate cravings or cells can go wild. Isothiocyanates dampen those receptors to moderate also.

I could go on and on, but actually we have many built in protections that protect us from cancer, but somehow improper food chemistry, food we cannot properly metabolize and excrete the toxins of, can override the protection. Medicines are often made to block enzymes or promote enzymes, but medicines are designed off of food chemistry that also does this. So, if you eat the right food at the wrong time or the wrong food which you cannot properly metabolize, you can cause an increased risk of cancer. Our epigenetic factors are designed from our ancestors eating habits and environmental factors, so what they ate might be better tolerated because we have some protection built in. Too much change in our diets too quick, I am talking about quick being in two or three generations, can lead to increased cancer risk.

These are just some of the factors, Molybdenum enzymes can help to detox nitrosamines. But the enzyme is shared with other metabolic processes, you can only stretch it so far on each or combinations of these things. If you eat a lot of sulfites, like prunes and dates, there is less available for nitrates and nitrate detox and with nitrosamines that utilize the same systems. Now nitrates are found in lettuce, eating a salad with brats taxes the system, maybe having potato salad instead would be better at the picnic. Or better yet, corn on the cob, it contributes methyl to the body which can help detox nitrogen compounds. Corn on the cob goes great with BBQ spare ribs, there is a reason for that. The caffeine in coffee helps protect a person from the nitrogen compounds in spare ribs causing cancer too, and so can ethyl in the beer or drink you have with your spare ribs. the methyl in caffeine can also protect a person from some of the negative effects of cigarettes, and the cigarettes can break down the methyl in caffeine too.

It's late, I am getting a little tired, so if you want to pick my brain tomorrow, just ask another question and I will give you a long drawn out answer that strays all over the place like I always do. The answer is never simple when you deal with things like this unless you are very good at understanding highly scientific words and can apply that info to everyday life.